ID   Q6MQB3_BDEBA            Unreviewed;       277 AA.
AC   Q6MQB3;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   SubName: Full=Serine protease trypsin family {ECO:0000313|EMBL:CAE78534.1};
DE            EC=3.4.21.4 {ECO:0000313|EMBL:CAE78534.1};
GN   OrderedLocusNames=Bd0564 {ECO:0000313|EMBL:CAE78534.1};
OS   Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS   HD100).
OC   Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC   Pseudobdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=264462 {ECO:0000313|EMBL:CAE78534.1, ECO:0000313|Proteomes:UP000008080};
RN   [1] {ECO:0000313|EMBL:CAE78534.1, ECO:0000313|Proteomes:UP000008080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100
RC   {ECO:0000313|Proteomes:UP000008080};
RX   PubMed=14752164; DOI=10.1126/science.1093027;
RA   Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA   Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA   Schuster S.C.;
RT   "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT   genomic perspective.";
RL   Science 303:689-692(2004).
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|ARBA:ARBA00007664}.
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DR   EMBL; BX842647; CAE78534.1; -; Genomic_DNA.
DR   RefSeq; WP_011163136.1; NC_005363.1.
DR   AlphaFoldDB; Q6MQB3; -.
DR   STRING; 264462.Bd0564; -.
DR   KEGG; bba:Bd0564; -.
DR   eggNOG; COG5640; Bacteria.
DR   HOGENOM; CLU_073536_0_0_7; -.
DR   Proteomes; UP000008080; Chromosome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR   PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:CAE78534.1};
KW   Protease {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:CAE78534.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008080};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..277
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004276779"
FT   DOMAIN          36..269
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   277 AA;  30172 MW;  7ED6A0076F963BB2 CRC64;
     MKKCFLIFLF LLSACAPALQ EPVTEHLLQE DLDSAIVGGR RVRANDPRAN WVVMVRGTKG
     FFLFKGSGIC TGAFITEDIV LTAAHCVTEK GATYEVAYGL SPLEEKRKVI KIDKVLVHED
     YAPSTESLNP NDIALIKIRG TKPARLKVLG LQVEPPLEQP TTFLAIGYGN TAAGPKINER
     GILHSTPTII TDINDTHLIG NQRNGIGICQ GDSGGPLLKA DEKGEPAIIG ITHATFRYKG
     DPVNSNECYN RAAYVNIAHQ MAWIQKNVAL ISDEPLK
//